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Q6FWM7

- H2A1_CANGA

UniProt

Q6FWM7 - H2A1_CANGA

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Protein

Histone H2A.1

Gene

HTA1

Organism
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

Functioni

Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei120 – 1201Not ubiquitinatedCurated

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW

GO - Biological processi

  1. DNA repair Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2A.1
Gene namesi
Name:HTA1
Ordered Locus Names:CAGL0C04411g
OrganismiCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Taxonomic identifieri284593 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesNakaseomyces/Candida clade
ProteomesiUP000002428: Chromosome C

Subcellular locationi

GO - Cellular componenti

  1. nucleosome Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 131130Histone H2A.1PRO_0000055212Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei5 – 51N6-acetyllysineBy similarity
Modified residuei8 – 81N6-acetyllysineBy similarity
Modified residuei106 – 1061N5-methylglutamineBy similarity
Modified residuei128 – 1281PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA double-strand breaks (DSBs) generated by exogenous genotoxic agents and by stalled replication forks. Phosphorylation is dependent on the DNA damage checkpoint kinases MEC1/ATR and TEL1/ATM, spreads on either side of a detected DSB site and may mark the surrounding chromatin for recruitment of proteins required for DNA damage signaling and repair. Gamma-H2A is removed from the DNA prior to the strand invasion-primer extension step of the repair process and subsequently dephosphorylated by PPH3, a component of the histone H2A phosphatase complex (HTP-C). Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint (By similarity).By similarity
Acetylated by ESA1 to form H2AK4ac and H2AK7ac.By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Interactioni

Subunit structurei

The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.

Structurei

3D structure databases

ProteinModelPortaliQ6FWM7.
SMRiQ6FWM7. Positions 14-121.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi128 – 1292[ST]-Q motif

Domaini

The [ST]-Q motif constitutes a recognition sequence for kinases from the PI3/PI4-kinase family.

Sequence similaritiesi

Belongs to the histone H2A family.Curated

Phylogenomic databases

HOGENOMiHOG000234652.
InParanoidiQ6FWM7.
KOiK11251.
OMAiHLPKTES.
OrthoDBiEOG7GN30N.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR002119. Histone_H2A.
[Graphical view]
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00620. HISTONEH2A.
SMARTiSM00414. H2A. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00046. HISTONE_H2A. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6FWM7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGGKGGKAG SAAKASQTRS AKAGLTFPVG RVHRLLRRGN YAQRIGSGAP
60 70 80 90 100
VYLTAVLEYL AAEILELAGN AARDNKKSRI IPRHLQLAIR NDDELNKLLG
110 120 130
NVTIAQGGVL PNIHQNLLPK KSAKPSASQE L
Length:131
Mass (Da):13,873
Last modified:January 23, 2007 - v3
Checksum:iB3E1DC2B0D30652D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR380949 Genomic DNA. Translation: CAG58273.1.
RefSeqiXP_445367.1. XM_445367.1.

Genome annotation databases

GeneIDi2886776.
KEGGicgr:CAGL0C04411g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR380949 Genomic DNA. Translation: CAG58273.1 .
RefSeqi XP_445367.1. XM_445367.1.

3D structure databases

ProteinModelPortali Q6FWM7.
SMRi Q6FWM7. Positions 14-121.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 2886776.
KEGGi cgr:CAGL0C04411g.

Phylogenomic databases

HOGENOMi HOG000234652.
InParanoidi Q6FWM7.
KOi K11251.
OMAi HLPKTES.
OrthoDBi EOG7GN30N.

Family and domain databases

Gene3Di 1.10.20.10. 1 hit.
InterProi IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR002119. Histone_H2A.
[Graphical view ]
Pfami PF00125. Histone. 1 hit.
[Graphical view ]
PRINTSi PR00620. HISTONEH2A.
SMARTi SM00414. H2A. 1 hit.
[Graphical view ]
SUPFAMi SSF47113. SSF47113. 1 hit.
PROSITEi PS00046. HISTONE_H2A. 1 hit.
[Graphical view ]
ProtoNeti Search...

Entry informationi

Entry nameiH2A1_CANGA
AccessioniPrimary (citable) accession number: Q6FWM7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 70 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

In contrast to vertebrates and insects, its C-terminus is not monoubiquitinated.Curated

Caution

To ensure consistency between histone entries, we follow the 'Brno' nomenclature for histone modifications, with positions referring to those used in the literature for the 'closest' model organism. Due to slight variations in histone sequences between organisms and to the presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the actual positions of modified amino acids in the sequence generally differ. In this entry the following conventions are used: H2AK4ac = acetylated Lys-5; H2AK7ac = acetylated Lys-8; H2AS128ph = phosphorylated Ser-128.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3